ID EMD_HUMAN Reviewed; 254 AA. AC P50402; Q6FI02; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 234. DE RecName: Full=Emerin; GN Name=EMD; Synonyms=EDMD, STA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Teratocarcinoma; RX PubMed=7894480; DOI=10.1038/ng1294-323; RA Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G., RA Toniolo D.; RT "Identification of a novel X-linked gene responsible for Emery-Dreifuss RT muscular dystrophy."; RL Nat. Genet. 8:323-327(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8733135; DOI=10.1093/hmg/5.5.659; RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six candidate RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."; RL Hum. Mol. Genet. 5:659-668(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8655156; DOI=10.1007/bf02281886; RA Yamada T., Kobayashi T.; RT "A novel emerin mutation in a Japanese patient with Emery-Dreifuss muscular RT dystrophy."; RL Hum. Genet. 97:693-694(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8595407; DOI=10.1093/hmg/4.10.1859; RA Bione S., Small K., Aksmanovic M.A., D'Urso M., Ciccodicola A., Merlini L., RA Morandi L., Kress W., Yates J.R.W., Warren S.T., Toniolo D.; RT "Identification of new mutations in the Emery-Dreifuss muscular dystrophy RT gene and evidence for genetic heterogeneity of the disease."; RL Hum. Mol. Genet. 4:1859-1863(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 1-17. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [11] RP PROTEIN SEQUENCE OF 1-31; 37-45; 48-115 AND 158-203, ACETYLATION AT MET-1, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma, and Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [12] RP SUBCELLULAR LOCATION. RX PubMed=9673989; DOI=10.1016/s0960-8966(98)00031-5; RA Squarzoni S., Sabatelli P., Ognibene A., Toniolo D., Cartegni L., RA Cobianchi F., Petrini S., Merlini L., Maraldi N.M.; RT "Immunocytochemical detection of emerin within the nuclear matrix."; RL Neuromuscul. Disord. 8:338-344(1998). RN [13] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=9472006; DOI=10.1242/jcs.111.6.781; RA Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.; RT "Aberrant intracellular targeting and cell cycle-dependent phosphorylation RT of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype."; RL J. Cell Sci. 111:781-792(1998). RN [14] RP INTERACTION WITH BANF1. RX PubMed=11792822; DOI=10.1242/jcs.114.24.4575; RA Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y., RA Yoneda Y., Wilson K.L., Hiraoka Y.; RT "BAF is required for emerin assembly into the reforming nuclear envelope."; RL J. Cell Sci. 114:4575-4585(2001). RN [15] RP INTERACTION WITH YTHDC1. RX PubMed=12755701; DOI=10.1046/j.1432-1033.2003.03617.x; RA Wilkinson F.L., Holaska J.M., Zhang Z., Sharma A., Manilal S., Holt I., RA Stamm S., Wilson K.L., Morris G.E.; RT "Emerin interacts in vitro with the splicing-associated factor, YT521-B."; RL Eur. J. Biochem. 270:2459-2466(2003). RN [16] RP INTERACTION WITH GMCL. RX PubMed=12493765; DOI=10.1074/jbc.m208811200; RA Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L.; RT "Transcriptional repressor germ cell-less (GCL) and barrier to RT autointegration factor (BAF) compete for binding to emerin in vitro."; RL J. Biol. Chem. 278:6969-6975(2003). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [18] RP INTERACTION WITH BCLAF1, AND CHARACTERIZATION OF VARIANT EDMD1 PHE-54. RX PubMed=15009215; DOI=10.1111/j.1432-1033.2004.04007.x; RA Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N., Mori C., RA Wilson K.L., Hiraoka Y.; RT "Emerin binding to Btf, a death-promoting transcriptional repressor, is RT disrupted by a missense mutation that causes Emery-Dreifuss muscular RT dystrophy."; RL Eur. J. Biochem. 271:1035-1045(2004). RN [19] RP FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF SER-196 RP AND SER-197, AND CHARACTERIZATION OF VARIANTS EDMD1 PHE-54; HIS-133 AND RP HIS-183. RX PubMed=15328537; DOI=10.1371/journal.pbio.0020231; RA Holaska J.M., Kowalski A.K., Wilson K.L.; RT "Emerin caps the pointed end of actin filaments: evidence for an actin RT cortical network at the nuclear inner membrane."; RL PLoS Biol. 2:1354-1362(2004). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [22] RP FUNCTION, AND INTERACTION WITH CTNNB1. RX PubMed=16858403; DOI=10.1038/sj.emboj.7601230; RA Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., RA Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V., RA Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.; RT "The inner nuclear membrane protein emerin regulates beta-catenin activity RT by restricting its accumulation in the nucleus."; RL EMBO J. 25:3275-3285(2006). RN [23] RP PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITH LMNA, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-49. RX PubMed=16972941; DOI=10.1111/j.1742-4658.2006.05464.x; RA Roberts R.C., Sutherland-Smith A.J., Wheeler M.A., Jensen O.N., RA Emerson L.J., Spiliotis I.I., Tate C.G., Kendrick-Jones J., Ellis J.A.; RT "The Emery-Dreifuss muscular dystrophy associated-protein emerin is RT phosphorylated on serine 49 by protein kinase A."; RL FEBS J. 273:4562-4575(2006). RN [24] RP FUNCTION. RX PubMed=16680152; DOI=10.1038/nature04682; RA Jacque J.-M., Stevenson M.; RT "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity."; RL Nature 441:641-645(2006). RN [25] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BETA-TUBULIN. RX PubMed=17785515; DOI=10.1083/jcb.200702026; RA Salpingidou G., Smertenko A., Hausmanowa-Petrucewicz I., Hussey P.J., RA Hutchison C.J.; RT "A novel role for the nuclear membrane protein emerin in association of the RT centrosome to the outer nuclear membrane."; RL J. Cell Biol. 178:897-904(2007). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; SER-60 AND RP SER-87, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [30] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LMNA. RX PubMed=19323649; DOI=10.1042/bc20080175; RA Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M., Schena E., RA Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.; RT "Emerin-prelamin A interplay in human fibroblasts."; RL Biol. Cell 101:541-554(2009). RN [31] RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=19167377; DOI=10.1016/j.ydbio.2008.12.038; RA Mamada H., Takahashi N., Taira M.; RT "Involvement of an inner nuclear membrane protein, Nemp1, in Xenopus neural RT development through an interaction with the chromatin protein BAF."; RL Dev. Biol. 327:497-507(2009). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-8 AND SER-171, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [36] RP INTERACTION WITH TMEM201. RX PubMed=21610090; DOI=10.1242/jcs.078923; RA Gudise S., Figueroa R.A., Lindberg R., Larsson V., Hallberg E.; RT "Samp1 is functionally associated with the LINC complex and A-type lamina RT networks."; RL J. Cell Sci. 124:2077-2085(2011). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [38] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [39] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-29; SER-49; SER-60; RP SER-87; SER-98; SER-171 AND SER-173, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [42] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [43] RP FUNCTION, AND INTERACTION WITH NEMP1. RX PubMed=32923640; DOI=10.1126/sciadv.abb4591; RA Tsatskis Y., Rosenfeld R., Pearson J.D., Boswell C., Qu Y., Kim K., RA Fabian L., Mohammad A., Wang X., Robson M.I., Krchma K., Wu J., RA Goncalves J., Hodzic D., Wu S., Potter D., Pelletier L., Dunham W.H., RA Gingras A.C., Sun Y., Meng J., Godt D., Schedl T., Ciruna B., Choi K., RA Perry J.R.B., Bremner R., Schirmer E.C., Brill J.A., Jurisicova A., RA McNeill H.; RT "The NEMP family supports metazoan fertility and nuclear envelope RT stiffness."; RL Sci. Adv. 6:eabb4591-eabb4591(2020). RN [44] RP STRUCTURE BY NMR OF 2-54. RX PubMed=11470279; DOI=10.1016/s0014-5793(01)02649-7; RA Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J., RA Zinn-Justin S.; RT "Structural analysis of emerin, an inner nuclear membrane protein mutated RT in X-linked Emery-Dreifuss muscular dystrophy."; RL FEBS Lett. 501:171-176(2001). RN [45] RP STRUCTURE BY NMR OF 2-54. RX PubMed=11435115; DOI=10.1016/s0969-2126(01)00611-6; RA Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I., RA Worman H.J., Zinn-Justin S.; RT "Structural characterization of the LEM motif common to three human inner RT nuclear membrane proteins."; RL Structure 9:503-511(2001). RN [46] RP VARIANTS EDMD1 HIS-183 AND THR-183. RX PubMed=10323252; DOI=10.1007/s004390050946; RA Ellis J.A., Yates J.R.W., Kendrick-Jones J., Brown C.A.; RT "Changes at P183 of emerin weaken its protein-protein interactions RT resulting in X-linked Emery-Dreifuss muscular dystrophy."; RL Hum. Genet. 104:262-268(1999). RN [47] RP VARIANT EDMD1 HIS-133. RX PubMed=11587540; DOI=10.1006/bbrc.2001.5708; RA Holt I., Clements L., Manilal S., Morris G.E.; RT "How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular RT dystrophy?"; RL Biochem. Biophys. Res. Commun. 287:1129-1133(2001). CC -!- FUNCTION: Stabilizes and promotes the formation of a nuclear actin CC cortical network. Stimulates actin polymerization in vitro by binding CC and stabilizing the pointed end of growing filaments. Inhibits beta- CC catenin activity by preventing its accumulation in the nucleus. Acts by CC influencing the nuclear accumulation of beta-catenin through a CRM1- CC dependent export pathway. Links centrosomes to the nuclear envelope via CC a microtubule association. Required for proper localization of non- CC farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear CC envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are CC cooperative cofactors of HIV-1 infection. Association of EMD with the CC viral DNA requires the presence of BAF and viral integrase. The CC association of viral DNA with chromatin requires the presence of BAF CC and EMD. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, CC ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, CC ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:32923640}. CC -!- SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and CC YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in CC the nuclear inner membrane. Interacts with SUN1 and SUN2 (By CC similarity). Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta- CC tubulin. Interacts with TMEM201. Interacts with NEMP1 CC (PubMed:32923640). {ECO:0000250|UniProtKB:O08579, CC ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12493765, CC ECO:0000269|PubMed:12755701, ECO:0000269|PubMed:15009215, CC ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16858403, CC ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:17785515, CC ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:21610090, CC ECO:0000269|PubMed:32923640}. CC -!- INTERACTION: CC P50402; Q9ULW3: ABT1; NbExp=6; IntAct=EBI-489887, EBI-2602396; CC P50402; P60709: ACTB; NbExp=2; IntAct=EBI-489887, EBI-353944; CC P50402; Q8WTP8: AEN; NbExp=3; IntAct=EBI-489887, EBI-8637627; CC P50402; P16157-17: ANK1; NbExp=3; IntAct=EBI-489887, EBI-941819; CC P50402; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-489887, EBI-7054139; CC P50402; Q5T686: AVPI1; NbExp=3; IntAct=EBI-489887, EBI-8640233; CC P50402; O75531: BANF1; NbExp=13; IntAct=EBI-489887, EBI-1055977; CC P50402; Q9NYF8: BCLAF1; NbExp=3; IntAct=EBI-489887, EBI-437804; CC P50402; Q8N7W2-2: BEND7; NbExp=9; IntAct=EBI-489887, EBI-10181188; CC P50402; Q13895: BYSL; NbExp=6; IntAct=EBI-489887, EBI-358049; CC P50402; Q8NEC5: CATSPER1; NbExp=9; IntAct=EBI-489887, EBI-744545; CC P50402; Q8N5R6: CCDC33; NbExp=3; IntAct=EBI-489887, EBI-740841; CC P50402; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-489887, EBI-12024864; CC P50402; P20138: CD33; NbExp=3; IntAct=EBI-489887, EBI-3906571; CC P50402; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-489887, EBI-739624; CC P50402; Q9HA82: CERS4; NbExp=3; IntAct=EBI-489887, EBI-2622997; CC P50402; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-489887, EBI-1045797; CC P50402; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-489887, EBI-17710733; CC P50402; P21964: COMT; NbExp=3; IntAct=EBI-489887, EBI-372265; CC P50402; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-489887, EBI-18013275; CC P50402; O43889-2: CREB3; NbExp=3; IntAct=EBI-489887, EBI-625022; CC P50402; P35222: CTNNB1; NbExp=3; IntAct=EBI-489887, EBI-491549; CC P50402; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-489887, EBI-12823659; CC P50402; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-489887, EBI-2349927; CC P50402; Q96PL5: ERMAP; NbExp=3; IntAct=EBI-489887, EBI-13361852; CC P50402; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-489887, EBI-18304435; CC P50402; Q969F0: FATE1; NbExp=10; IntAct=EBI-489887, EBI-743099; CC P50402; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-489887, EBI-3917143; CC P50402; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-489887, EBI-13345167; CC P50402; Q8IUY3: GRAMD2A; NbExp=3; IntAct=EBI-489887, EBI-11984319; CC P50402; O75031: HSF2BP; NbExp=3; IntAct=EBI-489887, EBI-7116203; CC P50402; Q0VD86: INCA1; NbExp=3; IntAct=EBI-489887, EBI-6509505; CC P50402; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-489887, EBI-749265; CC P50402; Q14500: KCNJ12; NbExp=3; IntAct=EBI-489887, EBI-11794596; CC P50402; B7U540: KCNJ18; NbExp=3; IntAct=EBI-489887, EBI-19949648; CC P50402; Q15842: KCNJ8; NbExp=3; IntAct=EBI-489887, EBI-17440235; CC P50402; Q9UGI6-2: KCNN3; NbExp=3; IntAct=EBI-489887, EBI-17888181; CC P50402; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-489887, EBI-8472129; CC P50402; P43628: KIR2DL3; NbExp=3; IntAct=EBI-489887, EBI-8632435; CC P50402; Q9H400: LIME1; NbExp=3; IntAct=EBI-489887, EBI-2830566; CC P50402; P02545: LMNA; NbExp=7; IntAct=EBI-489887, EBI-351935; CC P50402; P02545-1: LMNA; NbExp=4; IntAct=EBI-489887, EBI-351949; CC P50402; Q9P127: LUZP4; NbExp=9; IntAct=EBI-489887, EBI-10198848; CC P50402; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-489887, EBI-10268010; CC P50402; P50221: MEOX1; NbExp=3; IntAct=EBI-489887, EBI-2864512; CC P50402; P50222: MEOX2; NbExp=3; IntAct=EBI-489887, EBI-748397; CC P50402; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-489887, EBI-16439278; CC P50402; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-489887, EBI-6163737; CC P50402; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-489887, EBI-2514313; CC P50402; Q7Z6M4: MTERF4; NbExp=3; IntAct=EBI-489887, EBI-948435; CC P50402; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-489887, EBI-10247000; CC P50402; P35240-4: NF2; NbExp=3; IntAct=EBI-489887, EBI-1014514; CC P50402; Q9NQX5: NPDC1; NbExp=3; IntAct=EBI-489887, EBI-748927; CC P50402; Q9P286: PAK5; NbExp=3; IntAct=EBI-489887, EBI-741896; CC P50402; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-489887, EBI-2568609; CC P50402; Q04864-2: REL; NbExp=3; IntAct=EBI-489887, EBI-10829018; CC P50402; O60930: RNASEH1; NbExp=3; IntAct=EBI-489887, EBI-2372399; CC P50402; Q99962: SH3GL2; NbExp=2; IntAct=EBI-489887, EBI-77938; CC P50402; A6NEL2: SOWAHB; NbExp=3; IntAct=EBI-489887, EBI-23696033; CC P50402; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-489887, EBI-17280858; CC P50402; Q16623: STX1A; NbExp=3; IntAct=EBI-489887, EBI-712466; CC P50402; Q12846: STX4; NbExp=3; IntAct=EBI-489887, EBI-744942; CC P50402; Q9UH99: SUN2; NbExp=4; IntAct=EBI-489887, EBI-1044964; CC P50402; Q8NF91-3: SYNE1; NbExp=5; IntAct=EBI-489887, EBI-10760352; CC P50402; Q8NF91-11: SYNE1; NbExp=3; IntAct=EBI-489887, EBI-10758913; CC P50402; Q8WXH0-3: SYNE2; NbExp=5; IntAct=EBI-489887, EBI-10760388; CC P50402; Q7RTU1: TCF23; NbExp=3; IntAct=EBI-489887, EBI-12127592; CC P50402; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-489887, EBI-10276729; CC P50402; Q86VY9: TMEM200A; NbExp=3; IntAct=EBI-489887, EBI-11732844; CC P50402; Q5SNT2-2: TMEM201; NbExp=4; IntAct=EBI-489887, EBI-11994282; CC P50402; Q9BTV4: TMEM43; NbExp=5; IntAct=EBI-489887, EBI-721293; CC P50402; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-489887, EBI-18178701; CC P50402; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-489887, EBI-11742770; CC P50402; Q9Y320: TMX2; NbExp=3; IntAct=EBI-489887, EBI-6447886; CC P50402; Q9Y228: TRAF3IP3; NbExp=9; IntAct=EBI-489887, EBI-765817; CC P50402; Q8IWZ5: TRIM42; NbExp=6; IntAct=EBI-489887, EBI-5235829; CC P50402; O95292: VAPB; NbExp=3; IntAct=EBI-489887, EBI-1188298; CC P50402; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-489887, EBI-2555749; CC P50402; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-489887, EBI-12879708; CC P50402; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-489887, EBI-711679; CC P50402; P49910: ZNF165; NbExp=3; IntAct=EBI-489887, EBI-741694; CC P50402; Q53Z40: ZNF165; NbExp=3; IntAct=EBI-489887, EBI-10186058; CC P50402; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-489887, EBI-749023; CC P50402; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-489887, EBI-7233259; CC P50402; Q9BYN7: ZNF341; NbExp=3; IntAct=EBI-489887, EBI-9089622; CC P50402; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-489887, EBI-8643207; CC P50402; Q6P9A3: ZNF549; NbExp=3; IntAct=EBI-489887, EBI-13046342; CC P50402; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-489887, EBI-10251462; CC P50402; P68135: ACTA1; Xeno; NbExp=3; IntAct=EBI-489887, EBI-367540; CC P50402; Q9D666: Sun1; Xeno; NbExp=4; IntAct=EBI-489887, EBI-6752574; CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane CC {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; CC Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer CC membrane. Note=Colocalized with BANF1 at the central region of the CC assembling nuclear rim, near spindle-attachment sites. The accumulation CC of different intermediates of prelamin-A/C (non-farnesylated or CC carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its CC localization in the nucleus. CC -!- TISSUE SPECIFICITY: Skeletal muscle, heart, colon, testis, ovary and CC pancreas. CC -!- PTM: Found in four different phosphorylated forms, three of which CC appear to be associated with the cell cycle. CC {ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:9472006}. CC -!- DISEASE: Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1) CC [MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a CC degenerative myopathy characterized by weakness and atrophy of muscle CC without involvement of the nervous system, early contractures of the CC elbows, Achilles tendons and spine, and cardiomyopathy associated with CC cardiac conduction defects. {ECO:0000269|PubMed:10323252, CC ECO:0000269|PubMed:11587540, ECO:0000269|PubMed:15009215, CC ECO:0000269|PubMed:15328537}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=EMD db; Note=EMD mutation database; CC URL="https://databases.lovd.nl/shared/genes/EMD"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82434; CAA57817.1; -; mRNA. DR EMBL; L44140; AAA92645.1; -; Genomic_DNA. DR EMBL; D64111; BAA10972.1; -; Genomic_DNA. DR EMBL; X86810; CAA60500.1; -; Genomic_DNA. DR EMBL; BT007401; AAP36065.1; -; mRNA. DR EMBL; CR536536; CAG38773.1; -; mRNA. DR EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72742.1; -; Genomic_DNA. DR EMBL; BC000738; AAH00738.1; -; mRNA. DR CCDS; CCDS14745.1; -. DR PIR; S50834; S50834. DR RefSeq; NP_000108.1; NM_000117.2. DR PDB; 1JEI; NMR; -; A=2-54. DR PDB; 2ODC; NMR; -; I=2-47. DR PDB; 2ODG; NMR; -; C=2-47. DR PDB; 6GHD; X-ray; 2.10 A; G/H=2-45. DR PDB; 6RPR; X-ray; 2.26 A; G=2-44. DR PDB; 7NDY; X-ray; 1.44 A; G=2-187. DR PDBsum; 1JEI; -. DR PDBsum; 2ODC; -. DR PDBsum; 2ODG; -. DR PDBsum; 6GHD; -. DR PDBsum; 6RPR; -. DR PDBsum; 7NDY; -. DR AlphaFoldDB; P50402; -. DR BMRB; P50402; -. DR SMR; P50402; -. DR BioGRID; 108325; 789. DR CORUM; P50402; -. DR DIP; DIP-34638N; -. DR IntAct; P50402; 270. DR MINT; P50402; -. DR STRING; 9606.ENSP00000358857; -. DR GlyCosmos; P50402; 10 sites, 2 glycans. DR GlyGen; P50402; 11 sites, 2 O-linked glycans (11 sites). DR iPTMnet; P50402; -. DR MetOSite; P50402; -. DR PhosphoSitePlus; P50402; -. DR SwissPalm; P50402; -. DR BioMuta; EMD; -. DR DMDM; 1706639; -. DR EPD; P50402; -. DR jPOST; P50402; -. DR MassIVE; P50402; -. DR PaxDb; 9606-ENSP00000358857; -. DR PeptideAtlas; P50402; -. DR ProteomicsDB; 56218; -. DR Pumba; P50402; -. DR TopDownProteomics; P50402; -. DR Antibodypedia; 371; 534 antibodies from 40 providers. DR DNASU; 2010; -. DR Ensembl; ENST00000369842.9; ENSP00000358857.4; ENSG00000102119.12. DR Ensembl; ENST00000683627.1; ENSP00000507533.1; ENSG00000102119.12. DR GeneID; 2010; -. DR KEGG; hsa:2010; -. DR MANE-Select; ENST00000369842.9; ENSP00000358857.4; NM_000117.3; NP_000108.1. DR UCSC; uc004fkl.4; human. DR AGR; HGNC:3331; -. DR CTD; 2010; -. DR DisGeNET; 2010; -. DR GeneCards; EMD; -. DR GeneReviews; EMD; -. DR HGNC; HGNC:3331; EMD. DR HPA; ENSG00000102119; Low tissue specificity. DR MalaCards; EMD; -. DR MIM; 300384; gene. DR MIM; 310300; phenotype. DR neXtProt; NX_P50402; -. DR OpenTargets; ENSG00000102119; -. DR Orphanet; 98863; X-linked Emery-Dreifuss muscular dystrophy. DR PharmGKB; PA27766; -. DR VEuPathDB; HostDB:ENSG00000102119; -. DR eggNOG; ENOG502S5SJ; Eukaryota. DR GeneTree; ENSGT00390000002034; -. DR HOGENOM; CLU_095531_0_0_1; -. DR InParanoid; P50402; -. DR OMA; DGNPFWA; -. DR OrthoDB; 4123486at2759; -. DR PhylomeDB; P50402; -. DR TreeFam; TF337236; -. DR PathwayCommons; P50402; -. DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown. DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation. DR Reactome; R-HSA-4419969; Depolymerization of the Nuclear Lamina. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013405; RHOD GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR SignaLink; P50402; -. DR SIGNOR; P50402; -. DR BioGRID-ORCS; 2010; 10 hits in 783 CRISPR screens. DR ChiTaRS; EMD; human. DR EvolutionaryTrace; P50402; -. DR GeneWiki; Emerin; -. DR GenomeRNAi; 2010; -. DR Pharos; P50402; Tbio. DR PRO; PR:P50402; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P50402; Protein. DR Bgee; ENSG00000102119; Expressed in left ovary and 204 other cell types or tissues. DR ExpressionAtlas; P50402; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005635; C:nuclear envelope; IDA:LIFEdb. DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA. DR GO; GO:0005819; C:spindle; IBA:GO_Central. DR GO; GO:0160045; C:TMEM240-body; IEA:Ensembl. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL. DR GO; GO:0071763; P:nuclear membrane organization; IMP:FlyBase. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl. DR CDD; cd12939; LEM_emerin; 1. DR DisProt; DP01770; -. DR Gene3D; 1.10.720.40; -; 1. DR InterPro; IPR035004; Emerin. DR InterPro; IPR011015; LEM/LEM-like_dom_sf. DR InterPro; IPR003887; LEM_dom. DR InterPro; IPR034989; LEM_emerin. DR PANTHER; PTHR15171; EMERIN; 1. DR PANTHER; PTHR15171:SF2; EMERIN; 1. DR Pfam; PF03020; LEM; 1. DR SMART; SM00540; LEM; 1. DR SUPFAM; SSF63451; LEM domain; 1. DR PROSITE; PS50954; LEM; 1. DR Genevisible; P50402; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cardiomyopathy; KW Direct protein sequencing; Disease variant; KW Emery-Dreifuss muscular dystrophy; Membrane; Microtubule; Nucleus; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..254 FT /note="Emerin" FT /id="PRO_0000206140" FT TRANSMEM 223..243 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 1..45 FT /note="LEM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313" FT REGION 46..222 FT /note="Interaction with F-actin" FT /evidence="ECO:0000305" FT REGION 168..186 FT /note="Interaction with CTNNB1" FT /evidence="ECO:0000269|PubMed:16858403" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 49 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:16972941, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63190" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63190" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63190" FT MOD_RES 161 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O08579" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08579" FT VARIANT 54 FT /note="S -> F (in EDMD1; no loss of binding to F-actin, FT enhanced rate of actin polymerization and loss of binding FT to BCLAF1)" FT /evidence="ECO:0000269|PubMed:15009215, FT ECO:0000269|PubMed:15328537" FT /id="VAR_005198" FT VARIANT 133 FT /note="Q -> H (in EDMD1; loss of binding to F-actin)" FT /evidence="ECO:0000269|PubMed:11587540, FT ECO:0000269|PubMed:15328537" FT /id="VAR_016016" FT VARIANT 149 FT /note="D -> H (in dbSNP:rs2070818)" FT /id="VAR_038433" FT VARIANT 183 FT /note="P -> H (in EDMD1; no loss of binding to F-actin and FT enhanced rate of actin polymerization; dbSNP:rs104894805)" FT /evidence="ECO:0000269|PubMed:10323252, FT ECO:0000269|PubMed:15328537" FT /id="VAR_005199" FT VARIANT 183 FT /note="P -> T (in EDMD1; dbSNP:rs104894806)" FT /evidence="ECO:0000269|PubMed:10323252" FT /id="VAR_005200" FT MUTAGEN 49 FT /note="S->A: Abolishes phosphorylation. No effect on FT targeting to nuclear envelope nor on interaction with FT LMNA." FT /evidence="ECO:0000269|PubMed:16972941" FT MUTAGEN 49 FT /note="S->E: Mimics phosphorylation. No effect on targeting FT to nuclear envelope nor on interaction with LMNA." FT /evidence="ECO:0000269|PubMed:16972941" FT MUTAGEN 196 FT /note="S->A: No loss of binding to F-actin; when associated FT with A-197." FT /evidence="ECO:0000269|PubMed:15328537" FT MUTAGEN 197 FT /note="S->A: No loss of binding to F-actin; when associated FT with A-196." FT /evidence="ECO:0000269|PubMed:15328537" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:7NDY" FT HELIX 9..18 FT /evidence="ECO:0007829|PDB:7NDY" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:7NDY" FT HELIX 31..43 FT /evidence="ECO:0007829|PDB:7NDY" SQ SEQUENCE 254 AA; 28994 MW; EB62EDD59B7A044F CRC64; MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF FIYHFMQAEE GNPF //